LYS12/YIL094C Literature Guide Help

Other names published for LYS12: LYS10, LYS11, homoisocitrate dehydrogenase, YIL094C

LYS12 - Substrates/Ligands/Cofactors (9)

ReferenceOther Genes Addressed
Fazius F, et al.  (2012) The fungal a-aminoadipate pathway for lysine biosynthesis requires two enzymes of the aconitase family for the isomerization of homocitrate to homoisocitrate. Mol Microbiol 86(6):1508-30
Lin Y, et al.  (2009) Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry 48(30):7305-12
Lin Y, et al.  (2008) Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry 47(40):10809-15
Yamamoto T and Eguchi T  (2008) Thiahomoisocitrate: a highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. Bioorg Med Chem 16(6):3372-6
Lin Y, et al.  (2007) Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry 46(3):890-8
Yamamoto T, et al.  (2007) Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase. Bioorg Med Chem 15(3):1346-55
Bhattacharjee JK and Strassman M  (1967) Accumulation of tricarboxylic acids related to lysine biosynthesis in a yeast mutant. J Biol Chem 242(10):2542-6
Strassman M and Ceci LN  (1965) Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid. J Biol Chem 240(11):4357-61
Strassman M, et al.  (1964) Enzymatic conversion of homoisocitric acid into alpha-ketoadipic acid. Biochem Biophys Res Commun 14():268-71